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Regulation of G Protein-Coupled Receptors by Ubiquitination
#MMPMID28448471
Skieterska K
; Rondou P
; Van Craenenbroeck K
Int J Mol Sci
2017[Apr]; 18
(5
): ? PMID28448471
show ga
G protein-coupled receptors (GPCRs) comprise the largest family of membrane
receptors that control many cellular processes and consequently often serve as
drug targets. These receptors undergo a strict regulation by mechanisms such as
internalization and desensitization, which are strongly influenced by
posttranslational modifications. Ubiquitination is a posttranslational
modification with a broad range of functions that is currently gaining increased
appreciation as a regulator of GPCR activity. The role of ubiquitination in
directing GPCRs for lysosomal degradation has already been well-established.
Furthermore, this modification can also play a role in targeting membrane and
endoplasmic reticulum-associated receptors to the proteasome. Most recently,
ubiquitination was also shown to be involved in GPCR signaling. In this review,
we present current knowledge on the molecular basis of GPCR regulation by
ubiquitination, and highlight the importance of E3 ubiquitin ligases,
deubiquitinating enzymes and ?-arrestins. Finally, we discuss classical and
newly-discovered functions of ubiquitination in controlling GPCR activity.
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